CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001272
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 CAAX prenyl protease 1 homolog 
Protein Synonyms/Alias
 Farnesylated proteins-converting enzyme 1; FACE-1; Prenyl protein-specific endoprotease 1; Zinc metalloproteinase Ste24 homolog 
Gene Name
 ZMPSTE24 
Gene Synonyms/Alias
 FACE1; STE24 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
46QRQRRIYKTTTHVPPubiquitination[1, 2, 3, 4, 5, 6]
66MDSETFEKSRLYQLDubiquitination[1, 2, 3, 4, 5, 6, 7]
235PLPEGKLKEEIEVMAubiquitination[2, 4]
243EEIEVMAKSIDFPLTubiquitination[3]
251SIDFPLTKVYVVEGSubiquitination[1, 2, 3, 4, 5, 6]
259VYVVEGSKRSSHSNAubiquitination[2, 4]
314EGNSEEIKAKVKNKKubiquitination[2, 3, 5, 8]
316NSEEIKAKVKNKKQGubiquitination[4]
437DLYSALIKLNKDNLGubiquitination[1, 2, 5, 6, 9]
470LERLQALKTMKQH**ubiquitination[4]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [9] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 Proteolytically removes the C-terminal three residues of farnesylated proteins. Acts on lamin A/C. 
Sequence Annotation
 ACT_SITE 336 336
 ACT_SITE 419 419 Proton donor (By similarity).
 METAL 335 335 Zinc; catalytic.
 METAL 339 339 Zinc; catalytic.
 METAL 415 415 Zinc; catalytic.  
Keyword
 3D-structure; Complete proteome; Disease mutation; Endoplasmic reticulum; Hydrolase; Membrane; Metal-binding; Metalloprotease; Nucleus; Polymorphism; Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 475 AA 
Protein Sequence
MGMWASLDAL WEMPAEKRIF GAVLLFSWTV YLWETFLAQR QRRIYKTTTH VPPELGQIMD 60
SETFEKSRLY QLDKSTFSFW SGLYSETEGT LILLFGGIPY LWRLSGRFCG YAGFGPEYEI 120
TQSLVFLLLA TLFSALTGLP WSLYNTFVIE EKHGFNQQTL GFFMKDAIKK FVVTQCILLP 180
VSSLLLYIIK IGGDYFFIYA WLFTLVVSLV LVTIYADYIA PLFDKFTPLP EGKLKEEIEV 240
MAKSIDFPLT KVYVVEGSKR SSHSNAYFYG FFKNKRIVLF DTLLEEYSVL NKDIQEDSGM 300
EPRNEEEGNS EEIKAKVKNK KQGCKNEEVL AVLGHELGHW KLGHTVKNII ISQMNSFLCF 360
FLFAVLIGRK ELFAAFGFYD SQPTLIGLLI IFQFIFSPYN EVLSFCLTVL SRRFEFQADA 420
FAKKLGKAKD LYSALIKLNK DNLGFPVSDW LFSMWHYSHP PLLERLQALK TMKQH 475 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; IEA:Compara.
 GO:0008235; F:metalloexopeptidase activity; TAS:ProtInc.
 GO:0071586; P:CAAX-box protein processing; IEA:InterPro.
 GO:0006998; P:nuclear envelope organization; IEA:Compara.
 GO:0030327; P:prenylated protein catabolic process; IEA:Compara.
 GO:0006508; P:proteolysis; TAS:ProtInc. 
Interpro
 IPR027057; CAXX_Prtase_1.
 IPR001915; Peptidase_M48. 
Pfam
 PF01435; Peptidase_M48 
SMART
  
PROSITE
 PS00142; ZINC_PROTEASE 
PRINTS